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- EMDB-13210: Six-subunit hGID complex. -

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Entry
Database: EMDB / ID: EMD-13210
TitleSix-subunit hGID complex.
Map dataMap of the tetrameric assembly of the six-subunit hGID complex, processed in C2.
Sample
  • Complex: 6-subunit hGID
    • Protein or peptide: ARMC8beta
    • Protein or peptide: RanBP9
    • Protein or peptide: WDR26
    • Protein or peptide: Twa1
    • Protein or peptide: MAEA
    • Protein or peptide: RMND5A
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 24.0 Å
AuthorsMohamed WI / Park SL / Rabl J / Leitner A / Boehringer D / Peter M
Funding support Switzerland, 2 items
OrganizationGrant numberCountry
European Research Council (ERC)ITN network grant Switzerland
Swiss National Science Foundation Switzerland
Citation
Journal: EMBO Rep / Year: 2021
Title: The human GID complex engages two independent modules for substrate recruitment.
Authors: Weaam I Mohamed / Sophia L Park / Julius Rabl / Alexander Leitner / Daniel Boehringer / Matthias Peter /
Abstract: The human GID (hGID) complex is a conserved E3 ubiquitin ligase regulating diverse biological processes, including glucose metabolism and cell cycle progression. However, the biochemical function and ...The human GID (hGID) complex is a conserved E3 ubiquitin ligase regulating diverse biological processes, including glucose metabolism and cell cycle progression. However, the biochemical function and substrate recognition of the multi-subunit complex remain poorly understood. Using biochemical assays, cross-linking mass spectrometry, and cryo-electron microscopy, we show that hGID engages two distinct modules for substrate recruitment, dependent on either WDR26 or GID4. WDR26 and RanBP9 cooperate to ubiquitinate HBP1 in vitro, while GID4 is dispensable for this reaction. In contrast, GID4 functions as an adaptor for the substrate ZMYND19, which surprisingly lacks a Pro/N-end degron. GID4 substrate binding and ligase activity is regulated by ARMC8α, while the shorter ARMC8β isoform assembles into a stable hGID complex that is unable to recruit GID4. Cryo-EM reconstructions of these hGID complexes reveal the localization of WDR26 within a ring-like, tetrameric architecture and suggest that GID4 and WDR26/Gid7 utilize different, non-overlapping binding sites. Together, these data advance our mechanistic understanding of how the hGID complex recruits cognate substrates and provides insights into the regulation of its E3 ligase activity.
#1: Journal: Biorxiv / Year: 2021
Title: The human GID complex engages two independent modules for substrate recruitment
Authors: Mohamed WI / Park SL / Rabl J / Leitner A / Boehringer D / Peter M
History
DepositionJul 15, 2021-
Header (metadata) releaseOct 6, 2021-
Map releaseOct 6, 2021-
UpdateNov 17, 2021-
Current statusNov 17, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.015
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_13210.png

Downloads & links

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Map

FileDownload / File: emd_13210.map.gz / Format: CCP4 / Size: 8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMap of the tetrameric assembly of the six-subunit hGID complex, processed in C2.
Voxel sizeX=Y=Z: 4.25 Å
Density
Contour LevelBy AUTHOR: 0.015 / Movie #1: 0.015
Minimum - Maximum-0.054509643 - 0.085189015
Average (Standard dev.)0.00016637349 (±0.0033775307)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions128128128
Spacing128128128
CellA=B=C: 544.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z4.254.254.25
M x/y/z128128128
origin x/y/z0.0000.0000.000
length x/y/z544.000544.000544.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS128128128
D min/max/mean-0.0550.0850.000

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Supplemental data

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Half map: #1

Fileemd_13210_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_13210_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : 6-subunit hGID

EntireName: 6-subunit hGID
Components
  • Complex: 6-subunit hGID
    • Protein or peptide: ARMC8beta
    • Protein or peptide: RanBP9
    • Protein or peptide: WDR26
    • Protein or peptide: Twa1
    • Protein or peptide: MAEA
    • Protein or peptide: RMND5A

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Supramolecule #1: 6-subunit hGID

SupramoleculeName: 6-subunit hGID / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Complex of subunits WDR26, RanBP9, TWA1, MAEA, RMND5A, and ARMC8beta.
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm) / Recombinant strain: Sf9 / Recombinant cell: Sf9

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Macromolecule #1: ARMC8beta

MacromoleculeName: ARMC8beta / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDWSHPQFEK SAVDENLYFQ GGGRMEVTAS SRHYVDRLFD PDPQKVLQGV IDMKNAVIGN NKQKANLIVL GAVPRLLYLL QQETSSTELK TECAVVLGSL AMGTENNVKS LLDCHIIPAL LQGLLSPDLK FIEACLRCLR TIFTSPVTPE ELLYTDATVI PHLMALLSRS ...String:
MDWSHPQFEK SAVDENLYFQ GGGRMEVTAS SRHYVDRLFD PDPQKVLQGV IDMKNAVIGN NKQKANLIVL GAVPRLLYLL QQETSSTELK TECAVVLGSL AMGTENNVKS LLDCHIIPAL LQGLLSPDLK FIEACLRCLR TIFTSPVTPE ELLYTDATVI PHLMALLSRS RYTQEYICQI FSHCCKGPDH QTILFNHGAV QNIAHLLTSL SYKVRMQALK CFSVLAFENP QVSMTLVNVL VDGELLPQIF VKMLQRDKPI EMQLTSAKCL TYMCRAGAIR TDDNCIVLKT LPCLVRMCSK ERLLEERVEG AETLAYLIEP DVELQRIASI TDHLIAMLAD YFKYPSSVSA ITDIKRLDHD LKHAHELRQA AFKLYASLGA NDEDIRKKVS LGEGRPPVLT ASRQGVTST

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Macromolecule #2: RanBP9

MacromoleculeName: RanBP9 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MGSSHHHHHH SAVDENLYFQ GGGRMSGQPP PPPPQQQQQQ QQLSPPPPAA LAPVSGVVLP APPAVSAGSS PAGSPGGGAG GEGLGAAAAA LLLHPPPPPP PATAAPPPPP PPPPPPASAA APASGPPAPP GLAAGPGPAG GAPTPALVAG SSAAAPFPHG DSALNEQEKE ...String:
MGSSHHHHHH SAVDENLYFQ GGGRMSGQPP PPPPQQQQQQ QQLSPPPPAA LAPVSGVVLP APPAVSAGSS PAGSPGGGAG GEGLGAAAAA LLLHPPPPPP PATAAPPPPP PPPPPPASAA APASGPPAPP GLAAGPGPAG GAPTPALVAG SSAAAPFPHG DSALNEQEKE LQRRLKRLYP AVDEQETPLP RSWSPKDKFS YIGLSQNNLR VHYKGHGKTP KDAASVRATH PIPAACGIYY FEVKIVSKGR DGYMGIGLSA QGVNMNRLPG WDKHSYGYHG DDGHSFCSSG TGQPYGPTFT TGDVIGCCVN LINNTCFYTK NGHSLGIAFT DLPPNLYPTV GLQTPGEVVD ANFGQHPFVF DIEDYMREWR TKIQAQIDRF PIGDREGEWQ TMIQKMVSSY LVHHGYCATA EAFARSTDQT VLEELASIKN RQRIQKLVLA GRMGEAIETT QQLYPSLLER NPNLLFTLKV RQFIEMVNGT DSEVRCLGGR SPKSQDSYPV SPRPFSSPSM SPSHGMNIHN LASGKGSTAH FSGFESCSNG VISNKAHQSY CHSNKHQSSN LNVPELNSIN MSRSQQVNNF TSNDVDMETD HYSNGVGETS SNGFLNGSSK HDHEMEDCDT EMEVDSSQLR RQLCGGSQAA IERMIHFGRE LQAMSEQLRR DCGKNTANKK MLKDAFSLLA YSDPWNSPVG NQLDPIQREP VCSALNSAIL ETHNLPKQPP LALAMGQATQ CLGLMARSGI GSCAFATVED YLH

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Macromolecule #3: WDR26

MacromoleculeName: WDR26 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MGSSHHHHHH SAVDENLYFQ GGGRSQSDED VIRLIGQHLN GLGLNQTVDL LMQESGCRLE HPSATKFRNH VMEGDWDKAE NDLNELKPLV HSPHAIVVRG ALEISQTLLG IIVRMKFLLL QQKYLEYLED GKVLEALQVL RCELTPLKYN TERIHVLSGY LMCSHAEDLR ...String:
MGSSHHHHHH SAVDENLYFQ GGGRSQSDED VIRLIGQHLN GLGLNQTVDL LMQESGCRLE HPSATKFRNH VMEGDWDKAE NDLNELKPLV HSPHAIVVRG ALEISQTLLG IIVRMKFLLL QQKYLEYLED GKVLEALQVL RCELTPLKYN TERIHVLSGY LMCSHAEDLR AKAEWEGKGT ASRSKLLDKL QTYLPPSVML PPRRLQTLLR QAVELQRDRC LYHNTKLDNN LDSVSLLIDH VCSRRQFPCY TQQILTEHCN EVWFCKFSND GTKLATGSKD TTVIIWQVDP DTHLLKLLKT LEGHAYGVSY IAWSPDDNYL VACGPDDCSE LWLWNVQTGE LRTKMSQSHE DSLTSVAWNP DGKRFVTGGQ RGQFYQCDLD GNLLDSWEGV RVQCLWCLSD GKTVLASDTH QRIRGYNFED LTDRNIVQED HPIMSFTISK NGRLALLNVA TQGVHLWDLQ DRVLVRKYQG VTQGFYTIHS CFGGHNEDFI ASGSEDHKVY IWHKRSELPI AELTGHTRTV NCVSWNPQIP SMMASASDDG TVRIWGPAPF IDHQNIEEEC SSMDS

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Macromolecule #4: Twa1

MacromoleculeName: Twa1 / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MGSSHHHHHH SAVDENLYFQ GGGRMSYAEK PDEITKDEWM EKLNNLHVQR ADMNRLIMNY LVTEGFKEAA EKFRMESGIE PSVDLETLDE RIKIREMILK GQIQEAIALI NSLHPELLDT NRYLYFHLQQ QHLIELIRQR ETEAALEFAQ TQLAEQGEES RECLTEMERT ...String:
MGSSHHHHHH SAVDENLYFQ GGGRMSYAEK PDEITKDEWM EKLNNLHVQR ADMNRLIMNY LVTEGFKEAA EKFRMESGIE PSVDLETLDE RIKIREMILK GQIQEAIALI NSLHPELLDT NRYLYFHLQQ QHLIELIRQR ETEAALEFAQ TQLAEQGEES RECLTEMERT LALLAFDSPE ESPFGDLLHT MQRQKVWSEV NQAVLDYENR ESTPKLAKLL KLLLWAQNEL DQKKVKYPKM TDLSKGVIEE PK

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Macromolecule #5: MAEA

MacromoleculeName: MAEA / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDYKDDDDKS AVDENLYFQG GGRMAVQESA AQLSMTLKVQ EYPTLKVPYE TLNKRFRAAQ KNIDRETSHV TMVVAELEKT LSGCPAVDSV VSLLDGVVEK LSVLKRKAVE SIQAE DESA KLCKRRIEHL KEHSSDQPAA ASVWKRKRMD RMMVEHLLRC GYYNTAVKLA ...String:
MDYKDDDDKS AVDENLYFQG GGRMAVQESA AQLSMTLKVQ EYPTLKVPYE TLNKRFRAAQ KNIDRETSHV TMVVAELEKT LSGCPAVDSV VSLLDGVVEK LSVLKRKAVE SIQAE DESA KLCKRRIEHL KEHSSDQPAA ASVWKRKRMD RMMVEHLLRC GYYNTAVKLA RQSGIEDLVN IEMFLTAKEV EESLERRETA TCLAWCHDNK SRLRKMKSCL EFSLRIQEFI ELIRQNKRLD AVRHARKHFS QAEGSQLDEV RQAMGMLAFP PDTHISPYKD LLDPARWRML IQQFRYDNYR LHQLGNNSVF TLTLQAGLSA IKTPQCYKED GSSKSPDCPV CSRSLNKLAQ PLPMAHCANS RLVCKISGDV MNENNPPMML PNGYVYGYNS LLSIRQDDKV VCPRTKEVFH FSQAEKVYIM

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Macromolecule #6: RMND5A

MacromoleculeName: RMND5A / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MGSSHHHHHH SAVDENLYFQ GGGRMDQCVT VERELEKVLH KFSGYGQLCE RGLEELIDYT GGLKHEILQS HGQDAELSGT LSLVLTQCCK RIKDTVQKLA SDHKDIHSSV SRVGKAIDKN FDSDISSVGI DGCWQADSQR LLNEVMVEHF FRQGMLDVAE ELCQESGLSV ...String:
MGSSHHHHHH SAVDENLYFQ GGGRMDQCVT VERELEKVLH KFSGYGQLCE RGLEELIDYT GGLKHEILQS HGQDAELSGT LSLVLTQCCK RIKDTVQKLA SDHKDIHSSV SRVGKAIDKN FDSDISSVGI DGCWQADSQR LLNEVMVEHF FRQGMLDVAE ELCQESGLSV DPSQKEPFVE LNRILEALKV RVLRPALEWA VSNREMLIAQ NSSLEFKLHR LYFISLLMGG TTNQREALQY AKNFQPFALN HQKDIQVLMG SLVYLRQGIE NSPYVHLLDA NQWADICDIF TRDACALLGL SVESPLSVSF SAGCVALPAL INIKAVIEQR QCTGVWNQKD ELPIEVDLGK KCWYHSIFAC PILRQQTTDN NPPMKLVCGH IISRDALNKM FNGSKLKCPY CPMEQSPGDA KQIFF

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.1 mg/mL
BufferpH: 7.4
Component:
ConcentrationNameFormula
50.0 mMHEPES
200.0 mMsodium chlorideNaClSodium chloride
1.0 mMTCEP
0.05 %NP40

Details: 50 mM HEPES pH 7.4, 200 mM NaCl, 1mM TCEP and 0.05% NP40
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 1.0 nm
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
DetailsThe complex was purified with gel filtration and subsequently crosslinked using the GraFix method.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal magnification: 130000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 1-40 / Number grids imaged: 1 / Number real images: 3048 / Average exposure time: 8.5 sec. / Average electron dose: 80.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 73559
CTF correctionSoftware - Name: Gctf
Startup modelType of model: OTHER
Details: Used model of the five-subunit hGID assembly as initial model.
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final 3D classificationNumber classes: 100 / Avg.num./class: 736 / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C2 (2 fold cyclic) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 24.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 44062
FSC plot (resolution estimation)

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